Structural highlights
Function
[PORI_RHOCA] Forms channels that allow the passive diffusion of small hydrophilic solutes up to an exclusion limit of about 0.6 kDa.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of porin from Rhodobacter capsulatus has been refined using the simulated annealing method. The final model consists of all 301 amino acid residues well obeying standard geometry, three calcium ions, 274 solvent molecules, three detergent molecules and one unknown ligand modeled as a detergent molecule. The final crystallographic R-factor is 18.6% based on 42,851 independent reflections in the resolution range 10 to 1.8 A. The model is described in detail.
Structure of porin refined at 1.8 A resolution.,Weiss MS, Schulz GE J Mol Biol. 1992 Sep 20;227(2):493-509. PMID:1328651[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Weiss MS, Schulz GE. Structure of porin refined at 1.8 A resolution. J Mol Biol. 1992 Sep 20;227(2):493-509. PMID:1328651
